type	Journal Article
authors	Pathre, U.; Singh, A. K.; Sane, P. V.
title	Inactivation of leucine aminotransferase with diethylpyrocarbonate and rose bengal: evidence for an active site histidine residue
journal	Indian J Biochem Biophys
Activity	2.6.1.6
ui	90152711
year	(1989)
volume	26
number	3
pages	136-9.
keywords	Binding Sites
abstract	Modification of leucine aminotransferase by diethylpyrocarbonate or rose bengal-sensitized photo-oxidation caused rapid inactivation of the enzyme. The inactivation of leucine aminotransferase depended on the concentration of the reagent, the time of incubation and exhibited pseudo-first order kinetics. Rose bengal-sensitized photo-oxidation was maximum at pH 6.5 and 9. Substrates leucine and alpha-ketoglutarate protected the enzyme against inactivation by these reagents, thus suggesting participation of histidine residue at the substrate binding site.
last changed	2002/11/12 16:17